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Caspase-7

Definition:

Thiol protease involved in different programmed cell death processes, such as apoptosis, pyroptosis or granzyme-mediated programmed cell death, by proteolytically cleaving target proteins. Has a marked preference for Asp-Glu-Val-Asp (DEVD) consensus sequences, with some plasticity for alternate non-canonical sequences. Its involvement in the different programmed cell death processes is probably determined by upstream proteases that activate CASP7 (By similarity). Acts as an effector caspase involved in the execution phase of apoptosis: following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of proteins, such as CLSPN, PARP1, PTGES3 and YY1. Compared to CASP3, acts as a minor executioner caspase and cleaves a limited set of target proteins. Acts as a key regulator of the inflammatory response in response to bacterial infection by catalyzing cleavage and activation of the sphingomyelin phosphodiesterase SMPD1 in the extracellular milieu, thereby promoting membrane repair. Regulates pyroptosis in intestinal epithelial cells: cleaved and activated by CASP1 in response to S.typhimurium infection, promoting its secretion to the extracellular milieu, where it catalyzes activation of SMPD1, generating ceramides that repair membranes and counteract the action of gasdermin-D (GSDMD) pores (By similarity). Regulates granzyme-mediated programmed cell death in hepatocytes: cleaved and activated by granzyme B (GZMB) in response to bacterial infection, promoting its secretion to the extracellular milieu, where it catalyzes activation of SMPD1, generating ceramides that repair membranes and counteract the action of perforin (PRF1) pores (By similarity). Following cleavage by CASP1 in response to inflammasome activation, catalyzes processing and inactivation of PARP1, alleviating the transcription repressor activity of PARP1. Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction (By similarity). Cleaves and activates sterol regulatory element binding proteins (SREBPs). Cleaves phospholipid scramblase proteins XKR4, XKR8 and XKR9 (By similarity). In case of infection, catalyzes cleavage of Kaposi sarcoma-associated herpesvirus protein ORF57, thereby preventing expression of viral lytic genes.; [Isoform Beta]: Lacks enzymatic activity.

Referencias:

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[2]. Alexandre Desroches, et al. Characterization of caspase-7 interaction with RNA. Biochem J. 2021 Jul 16;478(13):2681-2696. [Content Brief]

[3]. Jeanne A Hardy, et al. Discovery of an allosteric site in the caspases. Proc Natl Acad Sci U S A. 2004 Aug 24;101(34):12461-6. [Content Brief]

[4]. Jean-Bernard Denault, et al. Engineered hybrid dimers: tracking the activation pathway of caspase-7. Mol Cell. 2006 Aug;23(4):523-33. [Content Brief]

[5]. Jean-Bernard Denault, et al. Human caspase-7 activity and regulation by its N-terminal peptide. J Biol Chem. 2003 Sep 5;278(36):34042-50. [Content Brief]

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[7]. T Fernandes-Alnemri, et al. Mch3, a novel human apoptotic cysteine protease highly related to CPP32. Cancer Res. 1995 Dec 15;55(24):6045-52. [Content Brief]

[8]. Catriona A L Clarke, et al. Cleavage of claspin by caspase-7 during apoptosis inhibits the Chk1 pathway. J Biol Chem. 2005 Oct 21;280(42):35337-45. [Content Brief]

[9]. Jeanne A Hardy, et al. Dissecting an allosteric switch in caspase-7 using chemical and mutational probes. J Biol Chem. 2009 Sep 18;284(38):26063-9. [Content Brief]

[10]. John G Walsh, et al. Executioner caspase-3 and caspase-7 are functionally distinct proteases. Proc Natl Acad Sci U S A. 2008 Sep 2;105(35):12815-9. [Content Brief]

[11]. Y Huang, et al. Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain. Cell. 2001 Mar 9;104(5):781-90. [Content Brief]

[12]. Hyo Jin Kang, et al. Structural asymmetry of procaspase-7 bound to a specific inhibitor. Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1514-21. [Content Brief]

[13]. Ting Peng, et al. Pathogen hijacks programmed cell death signaling by arginine ADPR-deacylization of caspases. Mol Cell. 2022 May 19;82(10):1806-1820.e8. [Content Brief]

[14]. Yaxin Liu, et al. Calmodulin Binding Activates Chromobacterium CopC Effector to ADP-Riboxanate Host Apoptotic Caspases. mBio. 2022 Jun 28;13(3):e0069022. [Content Brief]

[15]. Dave Boucher, et al. Caspase-7 uses an exosite to promote poly(ADP ribose) polymerase 1 proteolysis. Proc Natl Acad Sci U S A. 2012 Apr 10;109(15):5669-74. [Content Brief]

[16]. Scott J Eron, et al. Dual Site Phosphorylation of Caspase-7 by PAK2 Blocks Apoptotic Activity by Two Distinct Mechanisms. Structure. 2017 Jan 3;25(1):27-39. [Content Brief]

[17]. Nathan D Thomsen, et al. Structural snapshots reveal distinct mechanisms of procaspase-3 and -7 activation. Proc Natl Acad Sci U S A. 2013 May 21;110(21):8477-82. [Content Brief]

[18]. J A Lippke, et al. Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32. J Biol Chem. 1996 Jan 26;271(4):1825-8. [Content Brief]

[19]. Sarah Riman, et al. Phosphorylation of the transcription factor YY1 by CK2α prevents cleavage by caspase 7 during apoptosis. Mol Cell Biol. 2012 Feb;32(4):797-807. [Content Brief]

[20]. Süheda Erener, et al. Inflammasome-activated caspase 7 cleaves PARP1 to enhance the expression of a subset of NF-κB target genes. Mol Cell. 2012 Apr 27;46(2):200-11. [Content Brief]

[21]. Johnson Agniswamy, et al. Plasticity of S2-S4 specificity pockets of executioner caspase-7 revealed by structural and kinetic analysis. FEBS J. 2007 Sep;274(18):4752-65. [Content Brief]

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[23]. Bärbel Edelmann, et al. Caspase-8 and caspase-7 sequentially mediate proteolytic activation of acid sphingomyelinase in TNF-R1 receptosomes. EMBO J. 2011 Jan 19;30(2):379-94. [Content Brief]

[24]. Hirokazu Nakatsumi, et al. Identification of functional regions defining different activity in caspase-3 and caspase-7 within cells. J Biol Chem. 2010 Aug 13;285(33):25418-25. [Content Brief]

[25]. Jessica E Young, et al. Proteolytic cleavage of ataxin-7 by caspase-7 modulates cellular toxicity and transcriptional dysregulation. J Biol Chem. 2007 Oct 12;282(41):30150-60. [Content Brief]

[26]. T S Juan, et al. Identification and mapping of Casp7, a cysteine protease resembling CPP32 beta, interleukin-1 beta converting enzyme, and CED-3. Genomics. 1997 Feb 15;40(1):86-93. [Content Brief]

[27]. Alexandre Desroches, et al. Caspase-7 uses RNA to enhance proteolysis of poly(ADP-ribose) polymerase 1 and other RNA-binding proteins. Proc Natl Acad Sci U S A. 2019 Oct 22;116(43):21521-21528. [Content Brief]

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[29]. Vladimir Majerciak, et al. Caspase-7 cleavage of Kaposi sarcoma-associated herpesvirus ORF57 confers a cellular function against viral lytic gene expression. J Biol Chem. 2010 Apr 9;285(15):11297-307. [Content Brief]

[30]. A Rodríguez-Hernández, et al. Nuclear caspase-3 and caspase-7 activation, and poly(ADP-ribose) polymerase cleavage are early events in camptothecin-induced apoptosis. Apoptosis. 2006 Jan;11(1):131-9. [Content Brief]

[31]. Xiang Li, et al. Phosphorylation of caspase-7 by p21-activated protein kinase (PAK) 2 inhibits chemotherapeutic drug-induced apoptosis of breast cancer cell lines. J Biol Chem. 2011 Jun 24;286(25):22291-9. [Content Brief]

[32]. H Duan, et al. ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis. J Biol Chem. 1996 Jan 19;271(3):1621-5. [Content Brief]

[33]. J T Pai, et al. Purification and cDNA cloning of a second apoptosis-related cysteine protease that cleaves and activates sterol regulatory element binding proteins. Proc Natl Acad Sci U S A. 1996 May 28;93(11):5437-42. [Content Brief]

[34]. Cyrielle Martini, et al. Characterization of Hsp90 Co-Chaperone p23 Cleavage by Caspase-7 Uncovers a Peptidase-Substrate Interaction Involving Intrinsically Disordered Regions. Biochemistry. 2017 Sep 26;56(38):5099-5111. [Content Brief]

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